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Science 20 November 1998: Vol. 282. no. 5393, pp. 1511 - 1516 DOI: 10.1126/science.282.5393.1511
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Reports
The Role of Far1p in Linking the Heterotrimeric G Protein to Polarity Establishment Proteins During Yeast Mating
Anne-Christine Butty,
Peter M. Pryciak,
Linda S. Huang,
Ira Herskowitz,
Matthias Peter
*
Heterotrimeric guanosine triphosphate (GTP)-binding
proteins (G proteins) determine tissue and cell polarity in a variety of organisms. In yeast, cells orient polarized growth toward the mating
partner along a pheromone gradient by a mechanism that requires Far1p
and Cdc24p. Far1p bound G and interacted with polarity
establishment proteins, which organize the actin cytoskeleton. Cells
containing mutated Far1p unable to bind G or polarity establishment proteins were defective for orienting growth toward their
mating partner. In response to pheromones, Far1p moves from the nucleus
to the cytoplasm. Thus, Far1p functions as an adaptor that recruits
polarity establishment proteins to the site of extracellular signaling
marked by G to polarize assembly of the cytoskeleton in a
morphogenetic gradient.
A.-C. Butty and M. Peter, Swiss Institute for Experimental Cancer
Research (ISREC), Chemin des Boveresses 155, 1066 Epalinges/VD,
Switzerland. P. M. Pryciak, Department of Molecular Genetics and
Microbiology, University of Massachusetts Medical Center, Worcester
Foundation Campus, 222 Maple Avenue, Shrewsbury, MA 01545, USA. L. S. Huang and I. Herskowitz, Department of Biochemistry and Biophysics,
University of California, San Francisco, San Francisco, CA 94143-0448,
USA.
*
To whom correspondence should be addressed. E-mail:
matthias.peter{at}isrec.unil.ch
Read the Full Text
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